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AB89007

Recombinant human PRMT1 protein

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(2 Publications)

Recombinant human PRMT1 protein is a Human Full Length protein, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, FuncS.

View Alternative Names

HMT2, HRMT1L2, IR1B4, PRMT1, Protein arginine N-methyltransferase 1, Histone-arginine N-methyltransferase PRMT1, Interferon receptor 1-bound protein 4

1 Images
SDS-PAGE - Recombinant human PRMT1 protein (AB89007)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human PRMT1 protein (AB89007)

15% SDS-PAGE analysis of 3μg ab89007

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus MBP tag N-Terminus

Applications

SDS-PAGE, FuncS

applications

Biologically active

Yes

Biological activity

Specific Activity: 10,000unit/ml. Unit Definition : One unit will transfer 1pmol of methyl group to synthetic peptide of histone H4 for 10 minutes at 37C.

Accession

Q99873

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 40% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.484% Tris, 0.038% Magnesium chloride, 0.0308% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MHHHHHHMKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTNSSSNNNNNNNNNNLGIEGRGSHMAAAEAANCIMEVSCGQAESSEKPNAEDMTSKDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMFHNRHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIECSSISDYAVKIVKANKLDHVVTIIKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVLYARDKWLAPDGLIFPDRATLYVTAIEDRQYKDYKIHWWENVYGFDMSCIKDVAIKEPLVDVVDPKQLVTNACLIKEVDIYTVKVEDLTFTSPFCLQVKRNDYVHALVAYFNIEFTRCHKRTGFSTSPESPYTHWKQTVFYMEDYLTVKTGEEIFGTIGMRPNAKNNRDLDFTIDLDFKGQLCELSCSTDYRMR","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q99873","tags":[{"tag":"His","terminus":"N-Terminus"},{"tag":"MBP","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

PRMT1 also known as protein arginine methyltransferase 1 is an important enzyme for post-translational modification. With a molecular mass of approximately 41 kDa PRMT1 is involved in the methylation of arginine residues on target proteins. This enzyme is ubiquitously expressed across various tissues indicating its widespread importance in cellular functions. PRMT1 functions in both the nucleus and cytoplasm impacting diverse cellular processes through its enzymatic activity.
Biological function summary

PRMT1 participates in several essential cellular functions including signal transduction gene expression and RNA processing. It methylates histones and non-histone proteins influencing chromatin structure and function. PRMT1 does not normally function as part of a complex but it interacts individually with different substrates to exert its effects. PRMT1 activity is essential in regulating transcriptional activation and repression highlighting its significant role in cellular regulation.

Pathways

PRMT1 plays a central role in the regulation of the glucocorticoid receptor signaling and p53 pathways. In glucocorticoid receptor signaling PRMT1 modifies transcription factors affecting their ability to bind DNA and regulate gene expression. In the p53 pathway PRMT1 methylates p53 itself impacting cell cycle arrest and apoptotic functions. These pathways demonstrate PRMT1’s interaction with other proteins like the p53 protein highlighting its integrative role in essential cellular processes.

PRMT1 is implicated in cancer and cardiovascular diseases. Aberrant expression or activity of PRMT1 associates with tumor progression and poor prognosis in cancers making it a target for therapeutic intervention. Additionally PRMT1 contributes to the pathogenesis of cardiovascular diseases by influencing the expression of genes linked to cardiac hypertrophy. PRMT1 interacts with the p53 protein impacting cancer development while also being connected through its regulatory function on p53-associated genes in these diseases.

Specifications

Form

Liquid

Additional notes

ab89007 is purified using conventional chromatography techniques.

General info

Function

Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, FMR1, ILF3, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15, EWS, HABP4, SERBP1, RBM15, FOXO1, CHTOP, MAP3K5/ASK1, MICU1 and NPRL2 (PubMed : 10749851, PubMed : 15741314, PubMed : 16879614, PubMed : 18951090, PubMed : 22095282, PubMed : 25284789, PubMed : 26575292, PubMed : 26876602, PubMed : 27642082, PubMed : 30765518, PubMed : 31257072, PubMed : 38006878). Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation. May be involved in the regulation of TAF15 transcriptional activity, act as an activator of estrogen receptor (ER)-mediated transactivation, play a key role in neurite outgrowth and act as a negative regulator of megakaryocytic differentiation, by modulating p38 MAPK pathway. Methylates RBM15, promoting ubiquitination and degradation of RBM15 (PubMed : 26575292). Methylates MRE11 and TP53BP1, promoting the DNA damage response (PubMed : 15741314, PubMed : 16294045, PubMed : 29651020). Methylates FOXO1 and retains it in the nucleus increasing its transcriptional activity (PubMed : 18951090). Methylates CHTOP and this methylation is critical for its 5-hydroxymethylcytosine (5hmC)-binding activity (PubMed : 25284789). Methylates MAP3K5/ASK1 at 'Arg-78' and 'Arg-80' which promotes association of MAP3K5 with thioredoxin and negatively regulates MAP3K5 association with TRAF2, inhibiting MAP3K5 stimulation and MAP3K5-induced activation of JNK (PubMed : 22095282). Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (PubMed : 25284789). Plays a role in regulating alternative splicing in the heart (By similarity). Methylates NPRL2 at 'Arg-78' leading to inhibition of its GTPase activator activity and then the GATOR1 complex and consequently inducing timely mTORC1 activation under methionine-sufficient conditions (PubMed : 38006878).

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.

Post-translational modifications

Polyubiquitinated at Lys-145 by the SCF(FBXL17) complex, leading to its subsequent degradation (By similarity). Ubiquitination is regulated by acetylation at Lys-228 and Lys-233 (By similarity). Polyubiquitinated by E3 ubiquitin-protein ligase TRIM48, leading to suppression of MAP3K5/ASK1 methylation and subsequent MAP3K5 activation (PubMed:29186683).. Acetylation at Lys-228 and Lys-233 regulates ubiquitination by the SCF(FBXL17) complex. Acetylated at Lys-233 by p300/EP300. Deacetylated at Lys-228 and Lys-233 by SIRT1.

Subcellular localisation

Nucleus

Product protocols

Target data

Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, FMR1, ILF3, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15, EWS, HABP4, SERBP1, RBM15, FOXO1, CHTOP, MAP3K5/ASK1, MICU1 and NPRL2 (PubMed : 10749851, PubMed : 15741314, PubMed : 16879614, PubMed : 18951090, PubMed : 22095282, PubMed : 25284789, PubMed : 26575292, PubMed : 26876602, PubMed : 27642082, PubMed : 30765518, PubMed : 31257072, PubMed : 38006878). Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation. May be involved in the regulation of TAF15 transcriptional activity, act as an activator of estrogen receptor (ER)-mediated transactivation, play a key role in neurite outgrowth and act as a negative regulator of megakaryocytic differentiation, by modulating p38 MAPK pathway. Methylates RBM15, promoting ubiquitination and degradation of RBM15 (PubMed : 26575292). Methylates MRE11 and TP53BP1, promoting the DNA damage response (PubMed : 15741314, PubMed : 16294045, PubMed : 29651020). Methylates FOXO1 and retains it in the nucleus increasing its transcriptional activity (PubMed : 18951090). Methylates CHTOP and this methylation is critical for its 5-hydroxymethylcytosine (5hmC)-binding activity (PubMed : 25284789). Methylates MAP3K5/ASK1 at 'Arg-78' and 'Arg-80' which promotes association of MAP3K5 with thioredoxin and negatively regulates MAP3K5 association with TRAF2, inhibiting MAP3K5 stimulation and MAP3K5-induced activation of JNK (PubMed : 22095282). Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (PubMed : 25284789). Plays a role in regulating alternative splicing in the heart (By similarity). Methylates NPRL2 at 'Arg-78' leading to inhibition of its GTPase activator activity and then the GATOR1 complex and consequently inducing timely mTORC1 activation under methionine-sufficient conditions (PubMed : 38006878).
See full target information PRMT1

Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Cell reports 44:115205 PubMed39817908

2025

Opposing roles of p38α-mediated phosphorylation and PRMT1-mediated arginine methylation in driving TDP-43 proteinopathy.

Applications

Unspecified application

Species

Unspecified reactive species

Mari Aikio,Hana M Odeh,Heike J Wobst,Bo Lim Lee,Úna Chan,Jocelyn C Mauna,Korrie L Mack,Bradley Class,Thomas A Ollerhead,Alice F Ford,Edward M Barbieri,Ryan R Cupo,Lauren E Drake,Joshua L Smalley,Yuan-Ta Lin,Stephanie Lam,Reuben Thomas,Nicholas Castello,Ashmita Baral,Jenna N Beyer,Mohd A Najar,John Dunlop,Aaron D Gitler,Ashkan Javaherian,Julia A Kaye,George M Burslem,Dean G Brown,Christopher J Donnelly,Steven Finkbeiner,Stephen J Moss,Nicholas J Brandon,James Shorter

Nucleic acids research 50:11799-11819 PubMed36350639

2022

Type I arginine methyltransferases are intervention points to unveil the oncogenic Epstein-Barr virus to the immune system.

Applications

Unspecified application

Species

Unspecified reactive species

Gaelle Angrand,Alicia Quillévéré,Nadège Loaëc,Van-Trang Dinh,Ronan Le Sénéchal,Rahima Chennoufi,Patricia Duchambon,Marc Keruzoré,Rodrigo Prado Martins,Marie-Paule Teulade-Fichou,Robin Fåhraeus,Marc Blondel
View all publications

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